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PGM2 protein (Latimeria chalumnae) - STRING interaction network
"PGM2" - Phosphoglucomutase 2 in Latimeria chalumnae
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
PGM2Phosphoglucomutase 2; Belongs to the phosphohexose mutase family (537 aa)    
Predicted Functional Partners:
GPI
Glucose-6-phosphate isomerase; Belongs to the GPI family (555 aa)
   
 
  0.990
PGM1
Phosphoglucomutase 1; Belongs to the phosphohexose mutase family (593 aa)
   
  0.986
UGP2
UDP-glucose pyrophosphorylase 2a (507 aa)
   
  0.948
DERA
Deoxyribose-phosphate aldolase (putative) (320 aa)
   
 
  0.944
RPIA
Uncharacterized protein; Ribose 5-phosphate isomerase A (92 aa)
   
 
  0.933
TKT
Transketolase (626 aa)
   
  0.933
ENSLACG00000013076
Transketolase b (485 aa)
   
  0.933
RBKS
Ribokinase; Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5- phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway (317 aa)
   
 
  0.929
RASGRP2
Alpha-1,4 glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (1365 aa)
   
 
  0.927
PYGB
Alpha-1,4 glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (267 aa)
   
 
  0.926
Your Current Organism:
Latimeria chalumnae
NCBI taxonomy Id: 7897
Other names: L. chalumnae, Latimeria chalumnae, coelacanth
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